Some properties of the apoenzyme of NADPH-adreno-ferredoxin reductase from bovine adrenocortical mitochondria.
1. An apo-NADPH-adreno-ferredoxin reductase (EC 1.18.1.2) was obtained from bovine adrenocortical mitochondria and its physicochemical properties were investigated. 2. The effects of various substances such as NADPH, FAD and adreno-ferredoxin on the interaction of the apo-reductase were investigated by various column chromatographies. 3. The apo- and holo-reductases were found to be separated by adreno-ferredoxin affinity chromatography. 4. The removal of FAD from NADPH-adreno-ferredoxin reductase did not affect the net charge of the reductase. 5. The values of s20,w of apo- and holo-reductases were 3.8 x 10(-13) sec and 3.9 x 10(-13) sec, respectively. 6. The apo-reductase was more easily denatured by heat treatment than the holo-reductase. 7. FAD, and adreno-ferredoxin and both could protect the apo-reductase from thermal inactivation.
Yamazaki
M
M
Department of Biochemistry, Kagawa Medical School, Japan.
Ichikawa
Y
Y
D000302:Adrenal Cortex / Q000201:enzymology* / Q000648:ultrastructure; D000325:Adrenodoxin / Q000494:pharmacology; D000818:Animals; D001051:Apoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002845:Chromatography; D002846:Chromatography, Affinity; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry* / Q000302:isolation & purification; D005182:Flavin-Adenine Dinucleotide / Q000494:pharmacology; D006358:Hot Temperature; D008928:Mitochondria / Q000201:enzymology*; D009249:NADP / Q000494:pharmacology; D011489:Protein Denaturation
D001051:Apoenzymes; D000325:Adrenodoxin; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; D005287:Ferredoxin-NADP Reductase